The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
α-Keto acid dehydrogenase complexes
Abstract
Abstract The mammalian pyruvate dehydrogenase complex contains a core, consisting of dihydrolipoyl transacetylase, to which pyruvate dehydrogenase and dihydrolipoyl dehydrogenase (a flavoprotein) are joined. Electron microscopic studies indicated that the design of the transacetylase is based on icosahedral (532) symmetry and, therefore, it would be expected to contain 60 very similar, if not identical, polypeptide chains. Evidence is presented that the bovine kidney and heart dihydrolipoyl transacetylases are very similar and that each enzyme does indeed consist of 60 apparently identical polypeptide chains. Each chain apparently contains 1 molecule of covalently bound lipoic acid. The molecular weight of the transacetylase is about 3.12 ± 0.20 million. The pyruvate dehydrogenase components of the bovine kidney and heart pyruvate dehydrogenase complexes are also very similar. The uncomplexed enzymes have a molecular weight of about 154,000 and possess the subunit structure α2β2. The molecular weights of two subunits are about 41,000 and 36,000, respectively. Only the α-subunit undergoes phosphorylation in the presence of pyruvate dehydrogenase kinase and ATP. Possible functions of the two subunits are discussed. It appears that the bovine kidney and heart pyruvate dehydrogenase complexes contain about 60 pyruvate dehydrogenase units (αβ) but only 10–12 flavoprotein chains.
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Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 18,892
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,158
Automatic Recording Apparatus for Use in Chromatography of Amino Acids
Spackman, D. H., Stein, W. H., & Moore, S. (1958) · Analytical Chemistry · doi:10.1021/ac60139a006 · Cited by 9,585
A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures
Martin, R. G., & Ames, B. N. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64180-8 · Cited by 5,565
Equilibrium Ultracentrifugation of Dilute Solutions*
Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,384
Mans, R. J., & Novelli, G. D. (1961) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(61)90009-1 · Cited by 2,041
Swank, R. T., & Munkres, K. D. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90436-2 · Cited by 1,717
ENZYMATIC PROPERTIES OF THE INNER AND OUTER MEMBRANES OF RAT LIVER MITOCHONDRIA
Schnaitman, C., & Greenawalt, J. W. (1968) · The Journal of Cell Biology · doi:10.1083/jcb.38.1.158 · Cited by 1,386
Regulation of Metabolic Processes in Mitochondria
(1967) · Food and Cosmetics Toxicology · doi:10.1016/s0015-6264(67)83077-3 · Cited by 1,182
Cited by
Structure-function relationships in dihydrolipoamide acyltransferases.
Reed, L. J., & Hackert, M. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38795-2 · Cited by 377
Self-citationRegulation of skeletal muscle glycogen phosphorylase and PDH during maximal intermittent exercise
Parolin, M. L., Chesley, A., Matsos, M. P., Spriet, L. L., Jones, N. L., & Heigenhauser, G. J. F. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.5.e890 · Cited by 334
Brautigam, C. A., Wynn, R. M., Chuang, J. L., & Chuang, D. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806563200 · Cited by 70
Metadata
- Authors
- Barrera, C. R., Namihira, G., Hamilton, L., Munk, P., Eley, M. H., Linn, T. C., & Reed, L. J.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1972-02
- Volume
- 148
- Issue
- 2
- Pages
- 343-358
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1490403537
- Cited by
- 278
- References
- 33
- FWCI
- 5.83
- Type
- journal article
- Language
- en
- Open access
- closed
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